Results 191 to 200 of about 6,046 (231)
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Pseudoazurin–Nitrite Reductase Interactions
ChemBioChem, 2005AbstractThe nitrite reductase‐binding site on pseudoazurin has been determined by using NMR chemical‐shift perturbations. It comprises residues in the hydrophobic patch surrounding the exposed copper ligand His81 as well as several positively charged residues. The binding site is similar for both redox states of pseudoazurin, despite differences in the
Antonietta, Impagliazzo +2 more
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Denitrification and nitrite reduction: Pseudomonas aeruginosa nitrite-reductase
Biochimie, 1984Present knowledge of the different enzymatic steps of the denitrification chains in various bacteria, particularly Paracoccus denitrificans and Pseudomonas aeruginosa has been briefly reviewed. The question whether nitric oxide (NO), nitrous oxide (N2O) and other nitrogen derivatives are obligatory intermediates has been discussed.
Y, Henry, P, Bessières
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Regulation of nitrite uptake and nitrite reductase expression in Chlamydomonas reinhardtii
Biochimica et Biophysica Acta (BBA) - General Subjects, 1991Expression of nitrite uptake and nitrite reductase activities has been studied in Chlamydomonas reinhardtii under different nutritional conditions. Both activities were expressed at a low level in derepressed cells (with no nitrogen source) and at a high level in induced cells (with nitrate or nitrite).
A, Galván +3 more
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Stoichiometry of nitrite reduction catalyzed by Pseudomonas aeruginosa nitrite-reductase
Biochimie, 1984The stoichiometry of the reduction of nitrite catalyzed by Pseudomonas aeruginosa nitrite-reductase (cytochrome cd1) has been shown to yield nitrous oxide as the final product. Gas chromatography experiments demonstrated that nitric oxide is also formed as a free intermediate. A sequential formation of NO and N2O is discussed as opposed to the parallel
P, Bessières, Y, Henry
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A dissimilatory nitrite reductase in Paracoccus halodenitrificans
Archives of Microbiology, 1984Paracoccus halodenitrificans produced a membrane-associated nitrite reductase. Spectrophotometric analysis showed it to be associated with a cd-cytochrome and located on the inner side of the cytoplasmic membrane. When supplied with nitrite, membrane preparations produced nitrous oxide and nitric oxide in different ratios depending on the electron ...
M A, Grant, L I, Hochstein
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1971
Publisher Summary This chapter discusses the determination of nitrite reductase. The usual assay involves sodium dithionite as reductant and either ferredoxin or its artificial substitute, methyl viologen, as the electron carrier. Enzymatic activity can be best followed by measuring colorimetrically the rate of disappearance of nitrite.
Manuel Losada, Antonio Paneque
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Publisher Summary This chapter discusses the determination of nitrite reductase. The usual assay involves sodium dithionite as reductant and either ferredoxin or its artificial substitute, methyl viologen, as the electron carrier. Enzymatic activity can be best followed by measuring colorimetrically the rate of disappearance of nitrite.
Manuel Losada, Antonio Paneque
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Inheritance of Nitrite Reductase
1981Although nitrite reductase (NiR) resides primarily in the chloroplast (Dalling et al., 1972; Lips et al., 1972; Miflin, 1974; Ritenour et al., 1967; Washitani et al., 1977) it has not been determined whether this enzyme is coded for by chloroplast DNA or by nuclear DNA.
S. Heath-Pagliuso, R. C. Huffaker
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Structure of cytochrome c nitrite reductase
Nature, 1999The enzyme cytochrome c nitrite reductase catalyses the six-electron reduction of nitrite to ammonia as one of the key steps in the biological nitrogen cycle, where it participates in the anaerobic energy metabolism of dissimilatory nitrate ammonification.
Einsle, Oliver +6 more
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A nitrite reductase from Neurospora crassa
Biochimica et Biophysica Acta, 1960Abstract Nitrite reductase has been purified, over 50-fold from ordinary felts of Neurospora crassa, macroconidial wild type Em 5297a. The enzyme is a DPNH-dependent flavoprotein containing FAD, Fe and Cu and -SH groups. Copper may act by coupling the flavin component of the enzyme to nitrite since an external supply of Cu1+ reduced NO2 non ...
D J, NICHOLAS, A, MEDINA, O T, JONES
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The anoxic plant mitochondrion as a nitrite: NO reductase
Mitochondrion, 2011Under the conditions of oxygen deprivation, accumulating nitrite can be reduced in the mitochondrial electron transport chain forming free radical nitric oxide (NO). By reducing nitrite to NO, plant mitochondria preserve the capacity to oxidize external NADH and NADPH and retain a limited power for ATP synthesis complementing glycolytic ATP production.
Kapuganti J, Gupta, Abir U, Igamberdiev
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